Complementary approaches to obtaining thermodynamic parameters from protein ligand systems-challenges and opportunities

¹ ISIS Neutron and Muon Facility, STFC Rutherford Appleton Laboratory, Chilton, Didcot, OX11 0QX, UK
² Institute of Biological Information Processing (IBI-4: Biomacromolecular Systems and Processes) & JARA-SOFT, Forschungszentrum Jülich GmbH, D-52428 Jülich, Germany
³ Department für Chemie Physikalische Chemie, Universität zu Köln, 50939 Cologne, Germany
⁴ I. Physikalisches Institut (IA), AG Biophysik, RWTH Aachen, Sommerfeldstrasse 14, Aachen D-52074, Germany
⁵ Institute of Biological Information Processing (IBI-6: Molecular Biophysics), Forschungszentrum Jülich GmbH, D-52428 Jülich, Germany
⁶ Jülich Centre for Neutron Science (JCNS-1) and Institute of Biological Information Processing (IBI-8: Neutron Scattering and Soft Matter), Forschungszentrum Jülich GmbH, D-52428 Jülich, Germany
⁷ Institute of Physical Chemistry, RWTH Aachen University, Landoltweg 2, Aachen D-52056, Germany

^* Corresponding author: mona.sarter@stfc.ac.uk

Published online: 17 November 2022

Abstract

Protein ligand interactions play an important role in biology. Increasingly the aim is to understand and influence protein ligand binding. The binding process is heavily influenced by its thermodynamic parameters. In order to understand how the whole system thermodynamics work it is important to characterise the individual contribution of each of the systems components. While the change in conformational entropy of the protein can be determined using QENS complementary methods are necessary in order to characterise all components. This paper will describe the challenges that can occur when combining the different methods, as well as how they can be overcome.